ADH1A

Alcohol dehydrogenase 1A (class I), alpha polypeptide

PDB rendering based on 1deh.

Available structures
PDB	1HSO, 1U3T

Identifiers

Symbols

ADH1A; ADH1

External IDs

OMIM: 103700 HomoloGene: 88335 GeneCards: ADH1A Gene

EC number

1.1.1.1

Gene Ontology
Molecular function	• alcohol dehydrogenase activity, zinc-dependent • protein binding • zinc ion binding • oxidoreductase activity • metal ion binding
Cellular component	• cytoplasm • cytosol
Biological process	• alcohol metabolic process • ethanol oxidation • transcription, DNA-dependent • xenobiotic metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

n/a

n/a

RefSeq (mRNA)

NM_000667

n/a

RefSeq (protein)

NP_000658

n/a

Location (UCSC)

Chr 4:
100.2 – 100.21 Mb

n/a

PubMed search

[1]

n/a

Alcohol dehydrogenase 1A is an enzyme that in humans is encoded by the ADH1A gene.^[1]^[2]

This gene encodes class I alcohol dehydrogenase, alpha subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. Class I alcohol dehydrogenase, consisting of several homo- and heterodimers of alpha, beta, and gamma subunits, exhibits high activity for ethanol oxidation and plays a major role in ethanol catabolism. Three genes encoding alpha, beta and gamma subunits are tandemly organized in a genomic segment as a gene cluster. This gene is monomorphic and predominant in fetal and infant livers, whereas the genes encoding beta and gamma subunits are polymorphic and strongly expressed in adult livers.^[2]

References

^ Smith M (Mar 1986). "Genetics of human alcohol and aldehyde dehydrogenases". Adv Hum Genet 15: 249–90. PMID 3006456.
^ ^a ^b "Entrez Gene: ADH1A alcohol dehydrogenase 1A (class I), alpha polypeptide". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=124.

Lange LG, Sytkowski AJ, Vallee BL (1976). "Human liver alcohol dehydrogenase: purification, composition, and catalytic features.". Biochemistry 15 (21): 4687–93. doi:10.1021/bi00666a023. PMID 9982.
van Ooij C, Snyder RC, Paeper BW, Duester G (1992). "Temporal expression of the human alcohol dehydrogenase gene family during liver development correlates with differential promoter activation by hepatocyte nuclear factor 1, CCAAT/enhancer-binding protein alpha, liver activator protein, and D-element-binding protein". Mol. Cell. Biol. 12 (7): 3023–31. PMC 364516. PMID 1620113. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=364516.
Stewart MJ, McBride MS, Winter LA, Duester G (1990). "Promoters for the human alcohol dehydrogenase genes ADH1, ADH2, and ADH3: interaction of CCAAT/enhancer-binding protein with elements flanking the ADH2 TATA box". Gene 90 (2): 271–9. doi:10.1016/0378-1119(90)90190-3. PMID 2169444.
Yasunami M, Kikuchi I, Sarapata D, Yoshida A (1990). "The human class I alcohol dehydrogenase gene cluster: three genes are tandemly organized in an 80-kb-long segment of the genome". Genomics 7 (2): 152–8. doi:10.1016/0888-7543(90)90535-3. PMID 2347582.
Tsukahara M, Yoshida A (1989). "Chromosomal assignment of the alcohol dehydrogenase cluster locus to human chromosome 4q21-23 by in situ hybridization". Genomics 4 (2): 218–20. doi:10.1016/0888-7543(89)90304-2. PMID 2737681.
Matsuo Y, Yokoyama S (1989). "Molecular structure of the human alcohol dehydrogenase 1 gene". FEBS Lett. 243 (1): 57–60. doi:10.1016/0014-5793(89)81217-7. PMID 2920825.
Ikuta T, Szeto S, Yoshida A (1986). "Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence". Proc. Natl. Acad. Sci. U.S.A. 83 (3): 634–8. doi:10.1073/pnas.83.3.634. PMC 322918. PMID 2935875. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=322918.
von Bahr-Lindström H, Höög JO, Hedén LO, et al. (1986). "cDNA and protein structure for the alpha subunit of human liver alcohol dehydrogenase". Biochemistry 25 (9): 2465–70. doi:10.1021/bi00357a026. PMID 3013304.
Duester G, Farrés J, Felder MR, et al. (1999). "Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family". Biochem. Pharmacol. 58 (3): 389–95. doi:10.1016/S0006-2952(99)00065-9. PMID 10424757.
Rodriguez-Zavala JS, Weiner H (2002). "Structural aspects of aldehyde dehydrogenase that influence dimer-tetramer formation". Biochemistry 41 (26): 8229–37. doi:10.1021/bi012081x. PMID 12081471.
Sandberg M, Yasar U, Strömberg P, et al. (2003). "Oxidation of celecoxib by polymorphic cytochrome P450 2C9 and alcohol dehydrogenase". British journal of clinical pharmacology 54 (4): 423–9. doi:10.1046/j.1365-2125.2002.01660.x. PMC 1874434. PMID 12392591. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1874434.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Dannenberg LO, Chen HJ, Edenberg HJ (2006). "GATA-2 and HNF-3beta regulate the human alcohol dehydrogenase 1A (ADH1A) gene". DNA Cell Biol. 24 (9): 543–52. doi:10.1089/dna.2005.24.543. PMID 16153155.
Jelski W, Chrostek L, Szmitkowski M (2007). "The activity of class I, II, III, and IV of alcohol dehydrogenase isoenzymes and aldehyde dehydrogenase in pancreatic cancer". Pancreas 35 (2): 142–6. doi:10.1097/MPA.0b013e318053eae2. PMID 17632320.

PDB gallery

1deh: CRYSTALLIZATION OF HUMAN BETA1 ALCOHOL DEHYDROGENASE (15 MG/ML) IN 50 MM SODIUM PHOSPHATE (PH 7.5), 2.0 MM NAD+ AND 1 MM 4-IODOPYRAZOLE AT 25 OC, 13% (W/V) PEG 8000

1hdx: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES

1hdy: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES

1hdz: THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES

1hso: HUMAN ALPHA ALCOHOL DEHYDROGENASE (ADH1A)

1hsz: HUMAN BETA-1 ALCOHOL DEHYDROGENASE (ADH1B*1)

1ht0: HUMAN GAMMA-2 ALCOHOL DEHYDROGENSE

1htb: CRYSTALLIZATION OF HUMAN BETA3 ALCOHOL DEHYDROGENASE (10 MG/ML) IN 100 MM SODIUM PHOSPHATE (PH 7.5), 7.5 MM NAD+ AND 1 MM 4-IODOPYRAZOLE AT 25 C

1u3t: Crystal Structure of Human Alcohol Dehydrogenase Alpha-Alpha Isoform Complexed with N-Cyclopentyl-N-Cyclobutylformamide Determined to 2.5 Angstrom Resolution

1u3u: Crystal Structure of Human Alcohol Dehydrogenase Beta-1-Beta-1 Isoform Complexed with N-Benzylformamide Determined to 1.6 Angstrom Resolution

1u3v: Crystal Structure of Human Alcohol Dehydrogenase Beta-1-Beta-1 Isoform Complexed with N-Heptylformamide Determined to 1.65 Angstrom Resolution

1u3w: Crystal Structure of Human Alcohol Dehydrogenase Gamma-2-Gamma-2 Isoform Complexed with N-1-Methylheptylformamide Determined to 1.45 Angstrom Resolution

3hud: THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS

ADH1A

References

Further reading